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Open data
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Basic information
Entry | Database: PDB / ID: 1iv7 | ||||||
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Title | Crystal Structure of Single Chain Monellin | ||||||
![]() | Monellin | ||||||
![]() | PLANT PROTEIN / ALPHA+BETA | ||||||
Function / homology | ![]() Monellin, A chain / Monellin, A chain superfamily / Monellin, B chain / Monellin / Monellin / Nuclear Transport Factor 2; Chain: A, - #10 / Cystatin superfamily / Nuclear Transport Factor 2; Chain: A, / Roll / Alpha Beta Similarity search - Domain/homology | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Tamada, T. / Kato, Y. / Kuroki, R. | ||||||
![]() | ![]() Title: The Effect of Single Chain Derivatization on the Structure and Stability of the Monellin Authors: Kato, Y. / Tamada, T. / Sone, H. / Iijima, H. / Kuroki, R. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 53.8 KB | Display | ![]() |
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PDB format | ![]() | 39 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 375.4 KB | Display | ![]() |
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Full document | ![]() | 379.4 KB | Display | |
Data in XML | ![]() | 6 KB | Display | |
Data in CIF | ![]() | 9.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1iv9C ![]() 1molS C: citing same article ( S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 11287.853 Da / Num. of mol.: 2 / Mutation: E49N, N50E, E149N, N150E Source method: isolated from a genetically manipulated source Details: fusion protein concerning chain A comprise residues 1-50 (MONELLIN, CHAIN B) and 52-96 (MONELLIN, CHAIN A), Including glysine linker. fusion protein concerning chain B comprise residues 101- ...Details: fusion protein concerning chain A comprise residues 1-50 (MONELLIN, CHAIN B) and 52-96 (MONELLIN, CHAIN A), Including glysine linker. fusion protein concerning chain B comprise residues 101-150 (MONELLIN, CHAIN B) and 152-196 (MONELLIN, CHAIN A), Including glysine linker. Source: (gene. exp.) ![]() Plasmid: pST6311 / Species (production host): Escherichia coli Production host: ![]() ![]() Strain (production host): W3110 / References: UniProt: P02882, UniProt: P02881 #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.26 Å3/Da / Density % sol: 45.51 % |
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Crystal grow | Temperature: 277 K / Method: microbatch / pH: 7.2 Details: PEG8000, potassium phosphate, pH 7.2, micro batch, temperature 277K |
-Data collection
Diffraction | Mean temperature: 277 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IIC / Detector: IMAGE PLATE / Date: Mar 19, 1998 |
Radiation | Monochromator: MIRRORS / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→60 Å / Num. all: 18113 / Num. obs: 17026 / % possible obs: 94 % / Observed criterion σ(I): 0 / Rmerge(I) obs: 0.067 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1MOL Resolution: 1.82→15 Å / Cor.coef. Fo:Fc: 0.959 / Cor.coef. Fo:Fc free: 0.941 / SU B: 4.762 / SU ML: 0.136 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.162 / ESU R Free: 0.149 / Stereochemistry target values: MAXIMUM LIKELIHOOD
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 31.272 Å2
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Refinement step | Cycle: LAST / Resolution: 1.82→15 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.824→1.871 Å / Total num. of bins used: 20 /
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